[NMR paper] Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Related ArticlesEnhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
Chem Commun (Camb). 2013 Dec 23;
Authors: Helge Meyer N, Zangger K
Abstract
Limited spectral resolution in the proton dimension of NMR spectra is a severe problem in intrinsically disordered proteins. Here we show that homonuclear broadband proton decoupling of the direct and indirect dimensions of multi-dimensional NMR spectra significantly enhances their resolution.
PMID: 24366473 [PubMed - as supplied by publisher]
[NMR paper] Homonuclear decoupling for enhancing resolution and sensitivity in NOE and RDC measurements of peptides and proteins
Homonuclear decoupling for enhancing resolution and sensitivity in NOE and RDC measurements of peptides and proteins
Publication date: Available online 22 November 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Jinfa Ying , Julien Roche , Ad Bax</br>
Application of band-selective homonuclear (BASH) 1H decoupling pulses during acquisition of the 1H free induction decay is shown to be an efficient procedure for removal of scalar and residual dipolar couplings between amide and aliphatic protons. BASH decoupling can be applied in both dimensions of a...
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[NMR paper] Resonance assignment of the NMR spectra of disordered proteins using a multi-objective non-dominated sorting genetic algorithm.
Resonance assignment of the NMR spectra of disordered proteins using a multi-objective non-dominated sorting genetic algorithm.
Related Articles Resonance assignment of the NMR spectra of disordered proteins using a multi-objective non-dominated sorting genetic algorithm.
J Biomol NMR. 2013 Oct 17;
Authors: Yang Y, Fritzsching KJ, Hong M
Abstract
A multi-objective genetic algorithm is introduced to predict the assignment of protein solid-state NMR (SSNMR) spectra with partial resonance overlap and missing peaks due to broad linewidths,...
[NMR paper] Long-Observation-Window Band-Selective Homonuclear Decoupling: Increased Sensitivity and Resolution in Solid-State NMR Spectroscopy of Proteins
Long-Observation-Window Band-Selective Homonuclear Decoupling: Increased Sensitivity and Resolution in Solid-State NMR Spectroscopy of Proteins
Publication date: Available online 13 September 2013
Source:Journal of Magnetic Resonance</br>
Author(s): Jochem O. Struppe , Chen Yang , Yachong Wang , Roy V. Hernandez , Lisa M. Shamansky , Leonard J. Mueller</br>
Sensitivity and resolution are the two fundamental obstacles to extending solid-state nuclear magnetic resonance to even larger protein systems. Here, a novel long-observation-window band-selective...
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[NMR paper] Describing intrinsically disordered proteins at atomic resolution by NMR.
Describing intrinsically disordered proteins at atomic resolution by NMR.
Related Articles Describing intrinsically disordered proteins at atomic resolution by NMR.
Curr Opin Struct Biol. 2013 Mar 29;
Authors: Jensen MR, Ruigrok RW, Blackledge M
Abstract
There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from...
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Describing intrinsically disordered proteins at atomic resolution by NMR
Describing intrinsically disordered proteins at atomic resolution by NMR
Available online 29 March 2013
Publication year: 2013
Source:Current Opinion in Structural Biology</br>
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There is growing interest in the development of physical methods to study the conformational behaviour and biological activity of intrinsically disordered proteins (IDPs). In this review recent advances in the elucidation of quantitative descriptions of disordered proteins from nuclear magnetic resonance spectroscopy are presented. Ensemble approaches are particularly well adapted to map the...
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03-29-2013 07:52 PM
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
High dimensional and high resolution pulse sequences for backbone resonance assignment of intrinsically disordered proteins
Abstract Four novel 5D (HACA(N)CONH, HNCOCACB, (HACA)CON(CA)CONH, (H)NCO(NCA)CONH), and one 6D ((H)NCO(N)CACONH) NMR pulse sequences are proposed. The new experiments employ non-uniform sampling that enables achieving high resolution in indirectly detected dimensions. The experiments facilitate resonance assignment of intrinsically disordered proteins. The novel pulse sequences were successfully tested using δ subunit (20 kDa) of Bacillus subtilis RNA polymerase...
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[NMR paper] Assignment strategies in homonuclear three-dimensional 1H NMR spectra of proteins.
Assignment strategies in homonuclear three-dimensional 1H NMR spectra of proteins.
Related Articles Assignment strategies in homonuclear three-dimensional 1H NMR spectra of proteins.
Biochemistry. 1990 Feb 20;29(7):1829-39
Authors: Vuister GW, Boelens R, Padilla A, Kleywegt GJ, Kaptein R
The increase in dimensionality of three-dimensional (3D) NMR greatly enhances the spectral resolution in comparison to 2D NMR. It alleviates the problem of resonance overlap and may extend the range of molecules amenable to structure determination by...
Enhancing the resolution of multi-dimensional heteronuclear NMR spectra of intrinsically disordered proteins by homonuclear broadband decoupling.
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